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Volumn 4, Issue 9, 1997, Pages 739-743

The SH3 domain of Eps8 exists as a novel intertwined dimer

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN;

EID: 1842414289     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0997-739     Document Type: Article
Times cited : (78)

References (35)
  • 1
    • 0030585430 scopus 로고    scopus 로고
    • Solution structure and peptide binding of the SH3 domain from human Fyn
    • Morton, CJ. et al., Solution structure and peptide binding of the SH3 domain from human Fyn. Structure 4, 705-714 (1996).
    • (1996) Structure , vol.4 , pp. 705-714
    • Morton, C.J.1
  • 2
    • 0013484134 scopus 로고
    • Structural basis for the binding of proline rich peptides to SH3 domains
    • Yu, H. et al., Structural basis for the binding of proline rich peptides to SH3 domains. Cell 76, 933-945 (1994).
    • (1994) Cell , vol.76 , pp. 933-945
    • Yu, H.1
  • 4
    • 0027962645 scopus 로고
    • Two binding orientations for peptides to the Src SH3 domain: Development of a general model for SH3-ligand interaction
    • Feng, S., Chen, J.K., Yu, H., Simon, J.A. and Schreiber, S.L. Two binding orientations for peptides to the Src SH3 domain: development of a general model for SH3-ligand interaction. Science 266,1241-1247 (1994).
    • (1994) Science , vol.266 , pp. 1241-1247
    • Feng, S.1    Chen, J.K.2    Yu, H.3    Simon, J.A.4    Schreiber, S.L.5
  • 5
    • 0028485085 scopus 로고
    • High resolution crystal structures of tyrosine kinase SH3 domains complexed with proline rich peptides
    • Musacchio, A., Saraste, M. and Wilmanns, M. High resolution crystal structures of tyrosine kinase SH3 domains complexed with proline rich peptides. Nature Struct. Biol. 1, 546-551 (1994).
    • (1994) Nature Struct. Biol. , vol.1 , pp. 546-551
    • Musacchio, A.1    Saraste, M.2    Wilmanns, M.3
  • 6
    • 0028148629 scopus 로고
    • Structural determinants of peptide-binding orientation and of sequence specificity on SH3 domains
    • Lim, W.A., Richards, F.M. and Fox, R.O. Structural determinants of peptide-binding orientation and of sequence specificity on SH3 domains. Nature 372, 375-379 (1994).
    • (1994) Nature , vol.372 , pp. 375-379
    • Lim, W.A.1    Richards, F.M.2    Fox, R.O.3
  • 7
    • 0028675576 scopus 로고
    • Structure of the N-terminal SH3 domain of GRB2 complexed with a peptide from the guanine nucleotide releasing factor Sos
    • Terasawa, H. et al., Structure of the N-terminal SH3 domain of GRB2 complexed with a peptide from the guanine nucleotide releasing factor Sos. Nature Struct. Biol. 1, 891-897 (1994).
    • (1994) Nature Struct. Biol. , vol.1 , pp. 891-897
    • Terasawa, H.1
  • 8
    • 0028675698 scopus 로고
    • NMR structure of the N-terminal SH3 domain of GRB2 and its complex with a proline-rich peptide from SOS
    • Goudreau, N, et al., NMR structure of the N-terminal SH3 domain of GRB2 and its complex with a proline-rich peptide from SOS. Nature Struct Biol. 1, 898-907 (1994).
    • (1994) Nature Struct Biol. , vol.1 , pp. 898-907
    • Goudreau, N.1
  • 10
    • 0027245080 scopus 로고
    • Crystal structure of the SH3 domain in human Fyn: A comparison of the threedimensional structures of SH3 domains in tyrosine kinasesand spectrin
    • Noble, M.E.M., Musachio, A., Saraste, M., Courtneidge, S.A. and Wierenga, R.K. Crystal structure of the SH3 domain in human Fyn: a comparison of the threedimensional structures of SH3 domains in tyrosine kinasesand spectrin. EMBO J. 12, 2617-2624 (1993).
    • (1993) EMBO J. , vol.12 , pp. 2617-2624
    • Noble, M.E.M.1    Musachio, A.2    Saraste, M.3    Courtneidge, S.A.4    Wierenga, R.K.5
  • 11
    • 0027191192 scopus 로고
    • Solution structure and ligand binding site of the SH3 domain of the p85 alpha subunit of phosphoinositol 3-kinase
    • Booker,G.W. et al., Solution structure and ligand binding site of the SH3 domain of the p85 alpha subunit of phosphoinositol 3-kinase. Cell 73, 813-822 (1993).
    • (1993) Cell , vol.73 , pp. 813-822
    • Booker, G.W.1
  • 12
    • 0028288180 scopus 로고
    • Solution structure of GAP SH3 domain by 1H NMR and spatial arrangement of essential Ras signaling-involved sequence
    • Yang, Y.S. et al., Solution structure of GAP SH3 domain by 1H NMR and spatial arrangement of essential Ras signaling-involved sequence. EMBO J. 72, 1270-1279 (1994).
    • (1994) EMBO J. , vol.72 , pp. 1270-1279
    • Yang, Y.S.1
  • 13
    • 0027537997 scopus 로고
    • Solution structure of the SH3 domain of phospholipase-c gamma
    • Kohda, D. et al., Solution structure of the SH3 domain of phospholipase-c gamma. Cell 72, 953-960 (1993).
    • (1993) Cell , vol.72 , pp. 953-960
    • Kohda, D.1
  • 14
    • 0028351794 scopus 로고
    • The crystal structure of human CskSH3: Structural diversity near the RT-src and n-src loop
    • Borchert, T.V., Mathieu, M., Zeelen, J.P., Courtneidge, S.A. and Wierenga, R.K. The crystal structure of human CskSH3: structural diversity near the RT-src and n-src loop. FEBS Lett. 341, 79-85 (1994).
    • (1994) FEBS Lett. , vol.341 , pp. 79-85
    • Borchert, T.V.1    Mathieu, M.2    Zeelen, J.P.3    Courtneidge, S.A.4    Wierenga, R.K.5
  • 15
    • 0028774541 scopus 로고
    • Solution structure and ligand binding site of the carboxyterminal SH3 domain of GRB2
    • Kohda, D. et al., Solution structure and ligand binding site of the carboxyterminal SH3 domain of GRB2. Structure 2, 1029-1040 (1994).
    • (1994) Structure , vol.2 , pp. 1029-1040
    • Kohda, D.1
  • 16
    • 0027179703 scopus 로고
    • Eps8, a substrate for the epidermal growth factor receptor kinase, enhances EGF-dependent mitogenic signals
    • Fazioli, F. et al., Eps8, a substrate for the epidermal growth factor receptor kinase, enhances EGF-dependent mitogenic signals. EMBO J. 12, 3799-3808 (1993).
    • (1993) EMBO J. , vol.12 , pp. 3799-3808
    • Fazioli, F.1
  • 18
    • 0028922935 scopus 로고
    • Direct binding of Eps8 to the juxtamembrane domain of EGFR is phosphotyrosine and SH2 independent
    • Castagnino, P., Biesova, Z., Wong, W.T., Fazioli, F., Gill, G. and DiFiore, P.P. Direct binding of Eps8 to the juxtamembrane domain of EGFR is phosphotyrosine and SH2 independent- Oncogene 10, 723-729 (1995).
    • (1995) Oncogene , vol.10 , pp. 723-729
    • Castagnino, P.1    Biesova, Z.2    Wong, W.T.3    Fazioli, F.4    Gill, G.5    DiFiore, P.P.6
  • 19
    • 0029884459 scopus 로고    scopus 로고
    • RN-tre specifically binds to the SH3 domain of Eps8 with high affinity and confers growth advantage to NIH3T3 upon carboxy-terminal truncation
    • Matoskova, B., Wong, W.T., Nomura, N., Robbins, K.C. and Di Fiore, P.P. RN-tre specifically binds to the SH3 domain of Eps8 with high affinity and confers growth advantage to NIH3T3 upon carboxy-terminal truncation. Oncogene 12, 2679-2688 (1996).
    • (1996) Oncogene , vol.12 , pp. 2679-2688
    • Matoskova, B.1    Wong, W.T.2    Nomura, N.3    Robbins, K.C.4    Di Fiore, P.P.5
  • 20
    • 0028865843 scopus 로고
    • 3D domain swapping: A mechanism for oligomer assembly
    • Bennet, M.J., Schlunegger, M,P. and Eisenberg, D. 3D domain swapping: a mechanism for oligomer assembly. Prot Sci. 4, 2455-2468 (1995).
    • (1995) Prot Sci. , vol.4 , pp. 2455-2468
    • Bennet, M.J.1    Schlunegger, M.P.2    Eisenberg, D.3
  • 21
    • 0027749280 scopus 로고
    • Crystal structure of repetitive segments of spectrin
    • Y. Yan et al., Crystal structure of repetitive segments of spectrin. Science 262, 2027-2030 (1993).
    • (1993) Science , vol.262 , pp. 2027-2030
    • Yan, Y.1
  • 22
    • 0027482006 scopus 로고
    • Human CksHs2 atomic structure: A role for its hexameric assembly in cell cycle control
    • Parge, H.E., Arvai, A.S., Mustari, DJ., Reed, S.I. and Tainer, J.A. Human CksHs2 atomic structure: a role for its hexameric assembly in cell cycle control. Science 262, 387-395 (1993).
    • (1993) Science , vol.262 , pp. 387-395
    • Parge, H.E.1    Arvai, A.S.2    Mustari, D.J.3    Reed, S.I.4    Tainer, J.A.5
  • 23
    • 0025878347 scopus 로고
    • Pi-Pi interactions: The geometry and energetics of phenylalanine-phenylalanine interactions in proteins
    • Hunter, CA., Singh, J. and Thornton, J.M. Pi-Pi interactions: the geometry and energetics of phenylalanine-phenylalanine interactions in proteins. J. Mol. Biol. 218, 837-846 (1991).
    • (1991) J. Mol. Biol. , vol.218 , pp. 837-846
    • Hunter, C.A.1    Singh, J.2    Thornton, J.M.3
  • 24
    • 0029643950 scopus 로고
    • Structural basis for the specific interaction of lysine-containing prolinerich peptides with the N-terminal SH3 domain of c-CRK
    • Wu, X. et al., Structural basis for the specific interaction of lysine-containing prolinerich peptides with the N-terminal SH3 domain of c-CRK. Structure 3, 215-226(1995).
    • (1995) Structure , vol.3 , pp. 215-226
    • Wu, X.1
  • 25
    • 84988043558 scopus 로고
    • Molecular basis for interaction of the protein tyrosine kinase ZAP70 with the T-cell receptor
    • Hatada, M.H. et al., Molecular basis for interaction of the protein tyrosine kinase ZAP70 with the T-cell receptor. Nature 377, 835-837 (1995).
    • (1995) Nature , vol.377 , pp. 835-837
    • Hatada, M.H.1
  • 26
    • 0029036496 scopus 로고
    • Structural characterization of folded and unfolded states of and SH3 domain in equilibrium in aqueous buffer
    • Zhang, O. and Forman-Kay, J.D. Structural characterization of folded and unfolded states of and SH3 domain in equilibrium in aqueous buffer. Biochemistry 34, 6784-6792 (1995).
    • (1995) Biochemistry , vol.34 , pp. 6784-6792
    • Zhang, O.1    Forman-Kay, J.D.2
  • 27
    • 0029054142 scopus 로고
    • Constitutive phosphosphorylation of Eps8 in tumor cell lines: Relevance to malignant transformation
    • Matoskova, B., Wong, W.T., Salcini, A.E., Pelicci, P.G. and Di Fiore, P.P. Constitutive phosphosphorylation of Eps8 in tumor cell lines: relevance to malignant transformation. Mol. Cell. Biol. 15, 3805-3812 (1995).
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3805-3812
    • Matoskova, B.1    Wong, W.T.2    Salcini, A.E.3    Pelicci, P.G.4    Di Fiore, P.P.5
  • 28
    • 0025977037 scopus 로고
    • Eukaryotic proteins expressed in Escherichia coli: An improved thrombin cleavage and purification procedure of fusion proteins with glutathione-S-transferase
    • Guan, K.L and Dixon, J.E. Eukaryotic proteins expressed in Escherichia coli: an improved thrombin cleavage and purification procedure of fusion proteins with glutathione-S-transferase. Anal. Biochem. 192, 262-267 (1991).
    • (1991) Anal. Biochem. , vol.192 , pp. 262-267
    • Guan, K.L.1    Dixon, J.E.2
  • 30
    • 0028103275 scopus 로고
    • The CCP4 Suite: Programs for Protein Crystallography
    • The CCP4 Suite: Programs for Protein Crystallography. Acta Crystallogr. D50, 760 (1994).
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760
  • 32
    • 84945074880 scopus 로고
    • Conjugate-direction minimization: An improved method for the refinement of macromolecules
    • Tronrud, D.E. Conjugate-direction minimization: an improved method for the refinement of macromolecules. Acta Crystallogr. A48, 912-916 (1992).
    • (1992) Acta Crystallogr. , vol.A48 , pp. 912-916
    • Tronrud, D.E.1
  • 33
    • 0026597444 scopus 로고
    • The free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brunger, A.T. The free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 335, 472-474 (1992).
    • (1992) Nature , vol.335 , pp. 472-474
    • Brunger, A.T.1
  • 34
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and location of errors in these models
    • Jones, T.A., Zou,J.Y., Cowan, S.W. and Kjeldgaard, M. Improved methods for building protein models in electron density maps and location of errors in these models. Acta Oyst. A47, 110-119 (1991).
    • (1991) Acta Oyst. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 35
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases from partial structures with errors
    • Read, R.J. Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr. A42, 140-149 (1986).
    • (1986) Acta Crystallogr. , vol.A42 , pp. 140-149
    • Read, R.J.1


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